Structure-led protein engineering can expand the effector recognition profile of plant intracellular NLR immune receptors, providing a proof-of-principle for the development of novel disease resistance mechanisms in plants.
Structure/function studies of a plant pathogen effector in complex with a host disease resistance protein domain reveal the molecular basis for recognition and underpin future engineering of immunity in crops.
Allelic MLA immune receptors have an exceptional propensity to directly detect sequence-unrelated pathogen effectors and this feature might have facilitated functional diversification of the receptor in the host population.
Structures of the death domain of the p75 neurotrophin receptor in complex with downstream effectors show how competitive protein-protein interactions orchestrate the hierarchical activation of downstream pathways in non-catalytic receptors.
Generation of a highly deuterated 13C-methyl labeled wild-type GPCR sample is used to facilitate characterization of the molecular environments and fast ps-ns dynamics of sidechains when the receptor is bound to ligands of different efficacy.